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ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Active droplets through enzyme-free, dynamic phosphorylation.

Simone M Poprawa1, Michele Stasi1, Brigitte A K Kriebisch1

  • 1Department of Bioscience, Technical University of Munich, Lichtenbergstrasse 4, 85748, Garching, Germany.

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|May 17, 2024
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This summary is machine-generated.

Researchers developed an enzyme-free system for dynamic phosphorylation, mimicking biological energy transfer. This system controls peptide phase separation, creating active droplets fueled by continuous chemical reactions.

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Area of Science:

  • Biochemistry
  • Supramolecular Chemistry
  • Synthetic Biology

Background:

  • Life utilizes energy transduction via molecules like ATP to regulate protein function through phosphorylation.
  • Dynamic phosphorylation is a key biological process for regulating cellular functions.
  • Current synthetic systems lack enzyme-free methods for dynamic phosphorylation of supramolecular processes.

Purpose of the Study:

  • To develop an enzyme-free synthetic system for dynamic phosphorylation.
  • To investigate the regulation of supramolecular processes using energy stored in reactive molecules.
  • To model biological phosphorylation and explore protocell formation.

Main Methods:

  • An enzyme-free reaction cycle was designed using monoamidophosphate as the phosphorylating agent.
  • Histidine and histidine-containing peptides were transiently phosphorylated.
  • The lability and deactivation of phosphorylated species via hydrolysis were studied.
  • The system's tunability for different precursors and half-lives was assessed.
  • The effect of phosphorylated products on peptide phase separation was investigated.

Main Results:

  • An enzyme-free phosphorylation cycle was successfully established, consuming monoamidophosphate.
  • Phosphorylated histidine peptides were synthesized and shown to be labile, deactivating via hydrolysis.
  • The system demonstrated versatility and tunability in phosphorylating multiple precursors with controllable half-lives.
  • The phosphorylation products were shown to regulate peptide phase separation, forming active droplets.
  • These active droplets required continuous fuel conversion to maintain their structure.

Conclusions:

  • This study presents the first enzyme-free synthetic system for dynamic phosphorylation, offering a novel approach to supramolecular regulation.
  • The developed system serves as a valuable model for understanding biological phosphorylation mechanisms.
  • The findings provide insights into the formation and behavior of active droplets, relevant to protocell research.
  • The tunable nature of the system allows for diverse applications in synthetic biology and materials science.